来自大肠杆菌的RusA霍利迪连接体解离酶的结晶
Crystallization of RusA Holliday junction resolvase from Escherichia coli.
作者信息
Muranova Tatyana A, Sedelnikova Svetlana E, Leonard Philip M, Pasquo Alessandra, Bolt Edward L, Lloyd Robert G, Rafferty John B
机构信息
Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, Western Bank, Sheffield S10 2TN, England.
出版信息
Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2262-4. doi: 10.1107/s0907444903018948. Epub 2003 Nov 27.
Crystals of the Escherichia coli Holliday junction resolvase RusA have been obtained using the hanging-drop method and characterized. The crystals have a primitive monoclinic form and belong to space group P2(1). The V(M) value suggests the presence of two copies of the monomer in the asymmetric unit. A full three-wavelength MAD data collection on a selenomethionine-incorporated form has been undertaken and structure determination is under way using data collected to 2.1 A resolution.
利用悬滴法获得了大肠杆菌霍利迪连接体解离酶RusA的晶体并进行了表征。这些晶体呈原始单斜晶型，属于空间群P2(1)。V(M)值表明在不对称单元中存在两个单体拷贝。已对硒代甲硫氨酸掺入形式进行了完整的三波长MAD数据收集，目前正在使用收集到的分辨率为2.1埃的数据进行结构测定。
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